Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors

Nahoko Yamaji, Kenji Sugase, Terumi Nakajima, Takafumi Miki, Minoru Wakamori, Yasuo Mori, Takashi Iwashita

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Agelenin, isolated from the Agelenidae spider Agelena opulenta, is a peptide composed of 35 amino acids. We determined the three-dimensional structure of agelenin using two-dimensional NMR spectroscopy. The structure is composed of a short antiparallel β-sheet and four β-turns, which are stabilized by three disulfide bonds. Agelenin has characteristic residues, Phe9, Ser28 and Arg33, which are arranged similarly to the pharmacophore of the insect channel inhibitor, ω-atracotoxin-Hv1a. These observations suggest that agelenin and ω-atracotoxin-Hv1a bind to insect calcium channels in a similar manner. We also suggest that another mode of action may operate in the channel inhibition by ω-agatoxin-IVA and ω-atracotoxin-Hv2a.

Original languageEnglish
Pages (from-to)3789-3794
Number of pages6
JournalFEBS Letters
Volume581
Issue number20
DOIs
Publication statusPublished - 2007 Aug 7
Externally publishedYes

Keywords

  • Agelenin
  • Insect calcium channel
  • NMR
  • Spider toxin
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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